Nmr Spectral Acquisition
Nmr Spectral Acquisition - Related Videos
16:20
Hyperpolarized Xenon for NMR and MRI Applications
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Cited by 28 •
2012
The production of hyperpolarized xenon by means of spin exchange optical pumping (SEOP) is described. This method yields a ~10000-fold enhancement of the nuclear spin polarization of Xe-129 and has applications in nuclear magnetic resonance spectroscopy and imaging. Examples of gas phase and solution state experiments are given.
11:44
Spin Saturation Transfer Difference NMR (SSTD NMR): A New Tool to Obtain Kinetic Parameters of Chemical Exchange Processes
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Cited by 4 •
2016
A detailed protocol describing the SSTD NMR method is presented here to help new users apply this new method to obtain the kinetic parameters of their own systems undergoing chemical exchange.
04:33
Quantitative In-Cell Hydrogen NMR Spectroscopy to Monitor Protein-Ligand Interactions
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2025
In this video, we demonstrate the in-cell nuclear magnetic resonance spectroscopy technique to study protein-ligand interactions between unlabeled overexpressed proteins and small molecules. The successful ligand-protein interaction is confirmed visually by the appearance of an additional set of peaks in the spectral region of interest that gradually replaces the original peaks.
07:54
Assessing Hepatic Metabolic Changes During Progressive Colonization of Germ-free Mouse by 1H NMR Spectroscopy
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Cited by 6 •
2011
A progressive colonization procedure is described to further assess its impact on the host hepatic metabolism. Colonization is monitored non invasively by evaluating the urinary excretion of microbial co-metabolites by NMR-based metabolic profiling while hepatic metabolism is assessed by High Resolution Magic Angle Spinning (HR MAS) NMR profiling of intact biopsy.
08:54
NMR Spectroscopy as a Robust Tool for the Rapid Evaluation of the Lipid Profile of Fish Oil Supplements
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Cited by 21 •
2017
Here, high-resolution 1H and 13C Nuclear Magnetic Resonance (NMR) spectroscopy was used as a rapid and reliable tool for quantitative and qualitative analysis of encapsulated fish oil supplements.
FAQs
Pulse sequences determine how radiofrequency pulses perturb nuclear spin alignment and how the resulting signals are recorded. Different sequence choices can emphasize particular aspects of a sample’s chemical composition, molecular structure, or dynamics. Selecting an appropriate sequence therefore affects which molecular information becomes visible and helps match the acquisition to the scientific question.
Spectral width sets the frequency range captured during acquisition, while signal averaging combines repeated measurements to improve the resulting spectrum. These choices influence the balance between spectral coverage, sensitivity, and resolution. Researchers adjust them according to whether the experiment prioritizes observing a broad chemical profile or resolving weaker or closely spaced signals.
Relaxation delays provide time between acquisition events for nuclear spin populations to recover toward their prior state. The selected delay contributes to the quality and quantitative behavior of the recorded signals, while also affecting how efficiently measurements can be collected. Careful timing is therefore important when comparing samples or seeking reproducible spectral features.
Temperature is an acquisition condition that can influence both sensitivity and resolution. Maintaining a suitable, consistent temperature helps ensure that differences between spectra reflect sample composition or molecular behavior rather than uncontrolled measurement conditions. In studies of proteins, metabolites, or host-pathogen interactions, temperature should therefore be treated as part of the experimental design.
A typical workflow establishes the sample in a strong magnetic field, applies a selected radiofrequency pulse sequence, records the returning free induction decay, digitizes the signal, and converts it into a spectrum by Fourier transformation. Researchers then evaluate whether spectral width, relaxation delays, temperature, and signal averaging were appropriate for the intended structural or compositional analysis.
The resulting spectra can support studies of metabolites, proteins, host-pathogen interactions, and biochemical changes associated with disease or treatment. This makes the technique useful when investigators need molecular-level information about how biological samples differ across infection states or experimental conditions. The same acquisition framework can address composition, structure, and dynamics within these research contexts.
Acquisition can target nuclei such as 1H or 13C, allowing researchers to collect complementary signals from the same sample context. Those signals contribute to characterization of chemical composition and molecular structure, while appropriate acquisition settings determine the sensitivity and resolution obtained. Choosing the nucleus is therefore linked to the type of molecular information the experiment is designed to examine.